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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Updated: Jul 3, 2026

In Situ Characterization of Shewanella oneidensis MR1 Biofilms by SALVI and ToF-SIMS
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Published on: August 18, 2017

Validating annotations for uncharacterized proteins in Shewanella oneidensis.

Brenton Louie1, Peter Tarczy-Hornoch, Roger Higdon

  • 1Department of Medical Education and Biomedical Informatics, Division of Biomedical and Health Informatics, University of Washington, Seattle, Washington 98101-1304, USA.

Omics : a Journal of Integrative Biology
|August 9, 2008
PubMed
Summary
This summary is machine-generated.

Annotation databases accurately predict functions for uncharacterized proteins when experimental evidence exists. This study evaluated database performance, finding high accuracy and improved function prediction for proteins of unknown function.

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Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Proteomics

Background:

  • Uncharacterized proteins hinder molecular biology understanding.
  • Current function prediction methods rely on similarity searches but lack validated performance on unknown proteins.
  • Accurate functional annotation is crucial for biological discovery.

Purpose of the Study:

  • To evaluate the performance of commonly used annotation databases for predicting functions of uncharacterized proteins.
  • To develop a benchmark dataset for assessing annotation accuracy.
  • To determine the reliability of current annotation tools.

Main Methods:

  • Created a benchmark dataset of 30 previously uncharacterized proteins from Shewanella oneidensis with newly assigned functions.
  • Evaluated multiple annotation databases using this dataset.
  • Developed and applied 'conditional accuracy' as an evaluation metric.

Main Results:

  • Six annotation databases accurately predicted functions for at least 60% of the proteins.
  • Two databases achieved 90% conditional accuracy.
  • At least one database correctly predicted the function for 27 out of 30 proteins.

Conclusions:

  • Annotation databases effectively incorporate new experimental evidence.
  • These databases demonstrate accuracy in predicting functions for uncharacterized proteins.
  • Reliable function prediction is achievable when experimental evidence is available.